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Yorodumi- PDB-1zaj: Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zaj | ||||||
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Title | Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with mannitol-1,6-bisphosphate, a competitive inhibitor | ||||||
Components | Fructose-bisphosphate aldolase A | ||||||
Keywords | LYASE / aldolase / competitive inhibitor / non covalent complex / mannitol-1 / 6-bisphosphate / hexitol-1 | ||||||
Function / homology | Function and homology information negative regulation of Arp2/3 complex-mediated actin nucleation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / I band / glycolytic process / protein homotetramerization / positive regulation of cell migration Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.89 Å | ||||||
Authors | St-Jean, M. / Lafrance-Vanasse, J. / Liotard, B. / Sygusch, J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: High Resolution Reaction Intermediates of Rabbit Muscle Fructose-1,6-bisphosphate Aldolase: substrate cleavage and induced fit. Authors: St-Jean, M. / Lafrance-Vanasse, J. / Liotard, B. / Sygusch, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zaj.cif.gz | 346 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zaj.ent.gz | 275.5 KB | Display | PDB format |
PDBx/mmJSON format | 1zaj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/za/1zaj ftp://data.pdbj.org/pub/pdb/validation_reports/za/1zaj | HTTPS FTP |
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-Related structure data
Related structure data | 1zahC 1zaiC 1zalC 1adoS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is the homotetramer found in the asymmetric unit |
-Components
#1: Protein | Mass: 39263.672 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: ALDOA / Plasmid: pPB14 / Production host: Escherichia coli (E. coli) / Strain (production host): BL-21 SI (Invitrogen) / References: UniProt: P00883, fructose-bisphosphate aldolase #2: Chemical | ChemComp-M2P / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 46 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X8C / Wavelength: 0.9795 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 10, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. all: 135347 / Num. obs: 118124 / % possible obs: 87.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.172 / Χ2: 2.098 |
Reflection shell | Resolution: 1.75→1.81 Å / % possible obs: 46.3 % / Num. measured obs: 6216 / Χ2: 2.187 / % possible all: 46.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ADO Resolution: 1.89→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 1 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 81.193 Å2 | |||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.779 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.89→20 Å
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Refine LS restraints |
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Xplor file |
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